5UEA: Antigen-Fab complex with Histone chaperone ASF1

Structure of antigen-Fab complex with Histone chaperone ASF1. Determined by X-ray diffraction at 1.7 Å resolution. Released 10 Jan 2018.

Method: X-ray diffraction
Resolution: 1.7 Å
Organisms: Homo sapiens, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 6
Atoms: 9,775
Mol. weight: 130.63 kDa
Released: 10 Jan 2018

Explore 5UEA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UEA contains 44 α-helices and 109 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	10-12	3	2
β-strand	18-25	8	1
α-helix	29-31	3
β-strand	33-39	7	2
β-strand	45-51	7	2
β-strand	57-59	3	2
β-strand	64	1	1
β-strand	67-72	6	1
α-helix	73-75	3
β-strand	77-82	6	1
α-helix	84-86	3
β-strand	88-95	8	2
β-strand	102-103	2	2
β-strand	107-111	5	2
β-strand	116	1	3
α-helix	117-119	2
β-strand	120-124	5	4
β-strand	135-145	11	4
β-strand	146	1	3
β-strand	151-154	4	5
α-helix	155-157	3
β-strand	159	1	5
β-strand	163-165	3	4
α-helix	166-168	3
β-strand	169-170	2	4
β-strand	176-185	10	4
α-helix	186-188	3
β-strand	195-200	6	5
α-helix	201-203	3
β-strand	205-210	6	5

Chain B: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	20
β-strand	10-13	4	21
β-strand	19-25	7	20
β-strand	33-38	6	21
β-strand	45-49	5	21
β-strand	53-54	2	21
α-helix	55	1
β-strand	62-67	6	20
β-strand	70-75	6	20
α-helix	80-82	3
β-strand	85-90	6	21
β-strand	93	1	6
β-strand	97-98	2	21
β-strand	102-106	5	21
β-strand	111	1	22
α-helix	112-113	2
β-strand	114-118	5	23
α-helix	119-121	3
α-helix	122-127	6
β-strand	129-139	11	23
β-strand	140	1	22
β-strand	145-150	6	24
β-strand	153-154	2	24
α-helix	155	1
β-strand	159-163	5	23
α-helix	164-167	4
β-strand	173-182	10	23
α-helix	183-188	6
β-strand	191-197	7	24
β-strand	205-210	6	24

Chain D: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	13
β-strand	16-17	2	14
α-helix	21	1
β-strand	22-30	9	13
β-strand	38-45	8	14
β-strand	55-61	7	14
α-helix	64-65	2
β-strand	67-75	9	13
α-helix	76-79	3
β-strand	92-101	10	14
β-strand	104-117	14	14
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	14
β-strand	145-148	4	14

Chain H: 7 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	8
β-strand	10-12	3	9
β-strand	18-25	8	8
α-helix	29-31	3
β-strand	33-39	7	9
β-strand	46-51	6	9
β-strand	57-59	3	9
β-strand	67-72	6	8
α-helix	73-75	3
β-strand	77-82	6	8
α-helix	84-86	3
β-strand	88-95	8	9
β-strand	102-103	2	9
β-strand	107-111	5	9
β-strand	116	1	10
β-strand	120-124	5	11
β-strand	132	1	11
β-strand	135-145	11	11
β-strand	146	1	10
β-strand	151-154	4	12
α-helix	155-157	3
β-strand	163-165	3	11
α-helix	166-168	3
β-strand	169-170	2	11
β-strand	176-185	10	11
α-helix	186-190	5
β-strand	195-200	6	12
α-helix	201-203	3
β-strand	205-210	6	12

Chain L: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	15
β-strand	10-13	4	16
β-strand	19-25	7	15
β-strand	33-38	6	16
β-strand	45-49	5	16
β-strand	53-54	2	16
α-helix	55	1
β-strand	62-67	6	15
β-strand	70-75	6	15
α-helix	80-82	3
β-strand	84-90	7	16
β-strand	93	1	13
α-helix	96	1
β-strand	97-98	2	16
β-strand	102-106	5	16
β-strand	111	1	17
α-helix	112-113	2
β-strand	114-118	5	18
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	18
β-strand	140	1	17
β-strand	145-150	6	19
β-strand	153-154	2	19
α-helix	155	1
β-strand	159-163	5	18
α-helix	164-167	4
β-strand	173-182	10	18
α-helix	183-187	5
β-strand	191-197	7	19
β-strand	205-210	6	19

Chain X: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	6
β-strand	16-17	2	7
α-helix	21	1
β-strand	22-30	9	6
β-strand	38-45	8	7
β-strand	54-62	9	7
α-helix	65-66	2
β-strand	68-76	9	6
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-88	3
β-strand	93-101	9	7
β-strand	104-117	14	7
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	7
β-strand	145-148	4	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fab Heavy Chain	A, H	protein	229	Homo sapiens
Histone chaperone ASF1	D, X	protein	154	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P32447 (AlphaFold model)
Fab Light Chain	B, L	protein	215	Homo sapiens

Sequence of entity 1 (A, H), FASTA

>5UEA_1 Fab Heavy Chain (chains A, H)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSYSSIHWVRQAPGKGLEWVAYIYPSSGY
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSYSTKLAMDYWGQGTLVTV
VSRRLPPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS
SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Sequence of entity 2 (D, X), FASTA

>5UEA_2 Histone chaperone ASF1 (chains D, X)
GSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSI
LVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEE
ELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWD

Sequence of entity 3 (B, L), FASTA

>5UEA_3 Fab Light Chain (chains B, L)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQSQWYPITFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Primary citation

Antibody Switch Residue Engineering for Improved Crystallization Chaperones. Bailey, L.J., Kossiakoff, A.A. To be published.

Other PDB entries of the same protein (UniProt P32447 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1ROC 1.5 Å, Crystal structure of the histone deposition protein Asf1
5UCB 1.52 Å, Structure of antigen-Fab complex with engineered switch residue region.
2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
5UEK 1.7 Å, Structure of antigen-Fab 12E complex with Histone chaperone ASF1
6AYZ 2.1 Å, Crystal structure of Asf1-Fab 12E complex
2IDC 2.2 Å, Structure of the Histone H3-Asf1 Chaperone Interaction
4ZBJ 2.25 Å, UBN1 peptide bound to H3.3/H4/Asf1
4EO5 2.35 Å, Yeast Asf1 bound to H3/H4G94P mutant
5EII 2.44 Å, Structural determination of an protein complex of a Fab with increased solubility
6AZ2 2.48 Å, Crystal structure of Asf1-Fab 12E complex
4RRP 2.79 Å, Crystal Structure of the Fab complexed with antigen Asf1p, Northeast Structural Genomics…
9AWE 2.8 Å, The crystal structure of an engineered Protein GF with Human Kappa Fab

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